title: Characterization of protease activities in Capnocytophaga spp., Porphyromonas gingivalis, Prevotella spp., Treponema denticola and Actinobacillus actinomycetemcomitans.
abstract: Protease activities in cell sonicates of defined bacterial strains were examined using peptide substrates and class-specific inhibitors. Capnocytophaga spp. all produced serine dipeptidyl peptidase activity and arginine/lysine, elastase- and chymotrypsin-like enzymes with some metalloprotease characteristics. The elastase-like activity was strongest in Capnocytophaga sputigena, but the others were greatest in Capnocytophaga gingivalis. The latter also had a separate arginine-specific enzyme which appeared not to be present in the other two species. Porphyromonas gingivalis showed serine dipeptidyl peptidase activity and very strong arginine and lysine cysteine protease activities. Prevotella spp. had inhibitor-resistant dipeptidyl peptidase activity and arginine cysteine protease activity that was much weaker but biochemically similar to P. gingivalis. Treponema denticola possessed a strong trypsin-like serine protease activity as well as very weak dipeptidyl peptidase and chymotrypsin-like activities that were sensitive to some cysteine protease reagents. Actinobacillus actinomycetemcomitans showed a novel alanine- and lysine-specific activity, but its nature was unclear.
authors.affiliation: Department of Periodontology, King's College School of Medicine and Dentistry, London, United Kingdom.
authors.forename: M I
authors.initials: MI
authors.lastname: Gazi
authors.forename: S W
authors.initials: SW
authors.lastname: Cox
authors.forename: D T
authors.initials: DT
authors.lastname: Clark
authors.forename: B M
authors.initials: BM
authors.lastname: Eley
mesh_terms: D016976:Aggregatibacter actinomycetemcomitans / Q000201:enzymology*; D002206:Capnocytophaga / Q000201:enzymology*; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors / Q000378:metabolism; D010450:Endopeptidases / Q000145:classification / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism; D010510:Periodontal Diseases / Q000382:microbiology; D016966:Porphyromonas gingivalis / Q000201:enzymology*; D018720:Prevotella / Q000201:enzymology*; D011480:Protease Inhibitors / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000378:metabolism; D014208:Treponema / Q000201:enzymology*
chemical_list: D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D010450:Endopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases